Evidence map›Paper›PMID 33452620›Full record

ArticleMolecular and cellular biochemistry2021

Morphological study of TNPO3 and SRSF1 interaction during myogenesis by combining confocal, structured illumination and electron microscopy analysis.

Roberta Costa, Maria Teresa Rodia, Nicoletta Zini, Valentina Pegoraro, Roberta Marozzo, Cristina Capanni, Corrado Angelini, Giovanna Lattanzi, Spartaco Santi, Giovanna Cenacchi

Open access · hybridAbstract read
In one paragraph

Article in Molecular and cellular biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 18 citations in OpenAlex.

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  14. Inhibition of autophagy rescues muscle atrophy in a LGMDD2 Drosophila model.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Roberta Costa *Department of Biomedical and Neuromotor Sciences-DIBINEM, Alma Mater Studiorum University of Bologna, via Massarenti 9, 40138, Bologna, Italy.
Maria Teresa Rodia *Department of Biomedical and Neuromotor Sciences-DIBINEM, Alma Mater Studiorum University of Bologna, via Massarenti 9, 40138, Bologna, Italy.
Nicoletta ZiniCNR-National Research Council of Italy, Institute of Molecular Genetics "Luigi Luca Cavalli-Sforza", Unit of Bologna, via di Barbiano 1/10, 40136, Bologna, Italy.
Valentina PegoraroNeuromuscular Unit, Neurobiology Research group, IRCCS San Camillo Hospital, via Alberoni 70, 30126, Venice, Italy.
Roberta MarozzoNeuromuscular Unit, Neurobiology Research group, IRCCS San Camillo Hospital, via Alberoni 70, 30126, Venice, Italy.
Cristina CapanniCNR-National Research Council of Italy, Institute of Molecular Genetics "Luigi Luca Cavalli-Sforza", Unit of Bologna, via di Barbiano 1/10, 40136, Bologna, Italy.
Corrado AngeliniNeuromuscular Unit, Neurobiology Research group, IRCCS San Camillo Hospital, via Alberoni 70, 30126, Venice, Italy.
Giovanna LattanziCNR-National Research Council of Italy, Institute of Molecular Genetics "Luigi Luca Cavalli-Sforza", Unit of Bologna, via di Barbiano 1/10, 40136, Bologna, Italy.
Spartaco Santi *CNR-National Research Council of Italy, Institute of Molecular Genetics "Luigi Luca Cavalli-Sforza", Unit of Bologna, via di Barbiano 1/10, 40136, Bologna, Italy.
Giovanna Cenacchi *Department of Biomedical and Neuromotor Sciences-DIBINEM, Alma Mater Studiorum University of Bologna, via Massarenti 9, 40138, Bologna, Italy. giovanna.cenacchi@unibo.it.ORCID http://orcid.org/0000-0001-5824-3118
Istituto Ortopedico Rizzoli · ITIRCCS San Camillo Hospital · ITUniversity of Bologna · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transportin3 (TNPO3) shuttles the SR proteins from the cytoplasm to the nucleus. The SR family includes essential splicing factors, such as SRSF1, that influence alternative splicing, controlling protein diversity in muscle and satellite cell differentiation. Given the importance of alternative splicing in the myogenic process and in the maintenance of healthy muscle, alterations in the splicing mechanism might contribute to the development of muscle disorders. Combining confocal, structured illumination and electron microscopy, we investigated the expression of TNPO3 and SRSF1 during myogenesis, looking at nuclear and cytoplasmic compartments. We investigated TNPO3 and its interaction with SRSF1 and we observed that SRSF1 remained mainly localized in the nucleus, while TNPO3 decreased in the cytoplasm and was strongly clustered in the nuclei of differentiated myotubes. In conclusion, combining different imaging techniques led us to describe the behavior of TNPO3 and SRSF1 during myogenesis, showing that their dynamics follow the myogenic process and could influence the proteomic network necessary during myogenesis. The combination of different high-, super- and ultra-resolution imaging techniques led us to describe the behavior of TNPO3 and its interaction with SRSF1, looking at nuclear and cytoplasmic compartments. These observations represent a first step in understanding the role of TNPO3 and SRFSF1 in complex mechanisms, such as myogenesis.

Indexed as

Cell NucleusCytoplasmMuscle DevelopmentAnimalsbeta KaryopherinsCell LineMiceMicroscopy, ConfocalMicroscopy, ElectronSerine-Arginine Splicing Factorsbeta KaryopherinsSerine-Arginine Splicing FactorsSRSF1 protein, humanElectron microscopyMyogenesisSRSF1Structured illumination microscopyTNPO3

Identifiers

PMID33452620
PMCPMC7940345
OpenAlexW3119260683

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.